1. Volume 87, Issue 5, Pages 2990-2999 (November 2004)
Predicting the Three-Dimensional Structure of the Human Facilitative Glucose Transporter Glut1 by a Novel Evolutionary Homology Strategy: Insights on the Molecular Mechanism of Substrate Migration, and Binding Sites for Glucose and Inhibitory Molecules 
Alexis Salas-Burgos, Pavel Iserovich, Felipe Zuniga, Juan Carlos Vera, Jorge Fischbarg 
Biophysical Journal 
Volume 87, Issue 5, Pages (November 2004)
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2. Figure 1
Representations of Glut1. (a) Side view showing relative positions of the helices. Residues in red represent topology constraints derived from experimental results (explained in the text) involving N45, K300, and C429 for the extracellular side, and motifs 89RFGRR93 and 330RAGRR for the cytoplasmic side. Glut1 measures ∼35.6×26.3Å viewed from the top, and 46.2Å×27.2Å from the bottom. Its height is ∼61Å. (b) View from the extracellular side showing the tilt of the 12 transmembrane helices. X marks loops entering, whereas dots mark loops exiting. (c) Cytoplasmic view; marks as above. The helix colors are in concordance with the symmetry template found by Hirai et al. (2002). Figure drawn using PYMOL (
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3. Figure 2
Locations of pathologic mutants, residues crucial for activity, and surface calculated for the Glut1 transport pathway. (a) The backbone is represented in ribbons and colored as in Fig. 1. Residues are in space-filling mode and labeled; residues crucial for pathogenicity are in red, and those crucial for transport in blue. Cyan denotes a motif of two consecutive residues crucial for transport, and green denotes the Gln residues presumed involved in selectivity. The transport pathway is denoted by a surface representation in gray; it was calculated with the USF programs ( Kleywegt and Jones, 1994, 1996, 1999) and read in ccp4 format into the program used for this figure, VMD ( Humphrey et al., 1996). (b) Back view, using the same colors and representations.
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Copyright © 2004 The Biophysical Society Terms and Conditions

4. Figure 3
Side view to detail the helical ribbons surrounding the putative channel. Helix 1 not shown for clarity. Residues that affect Glut1 function upon mutation are highlighted (side chains shown as sticks). Residue coding: blue, crucial for transport; orange, tryptophans lining the channel (W388 and W412 are crucial for transport); and green, QLS and QLG motifs.
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5. Figure 4
Glut1 cavities before and after a 400-ps molecular dynamics simulation. (a) Starting conformation. Residues lining the transport pathway are colored in cyan. There are in addition several cavities facing the outside of the protein. The external cavity (magenta) is a continuation of the channel, separated from it by an obstruction or neck. There are other cavities, namely, a side cavity (red), and two cavities bound by charged residues including ATP binding motifs (Walker A, orange; Walker B, violet). (b) Conformation after 400ps. The pathway has expanded as the Walker B cavity has fused with it, but an internal cavity (magenta) has now appeared at the intracellular end of the channel, separated from it by a neck. The side cavity has divided into two: side cavity 1 (light red) and side cavity 2 (dark red). Figure drawn using KING (
Biophysical Journal  , DOI: ( /biophysj )
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6. Figure 5
Docking sites for substrates and characteristic inhibitors of Glut1. (a) Substrates and inhibitors at their docking sites. Slab view showing the cavities and transport pathway of Glut1. β-D-glucose (red) binds extracellularly, whereas both forskolin (green), and phloretin (magenta) bind at extracellular and intracellular sites. Cytochalasin B (blue) binds intracellularly. Figure drawn using SPDBV ( Guex and Peitsch, 1997). Docking sites for (b), glucose; (c) forskolin (extracellular); (d) phloretin (extracellular); (e) forskolin (intracellular); (f) phloretin (intracellular); and (g), cytochalasin B. White labels, residues; yellow sticks, hydrogen bonds. Numbers indicate Å distances.
Biophysical Journal  , DOI: ( /biophysj )
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